7aae: Difference between revisions
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<StructureSection load='7aae' size='340' side='right'caption='[[7aae]], [[Resolution|resolution]] 2.27Å' scene=''> | <StructureSection load='7aae' size='340' side='right'caption='[[7aae]], [[Resolution|resolution]] 2.27Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AAE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7aae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aae OCA], [https://pdbe.org/7aae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aae RCSB], [https://www.ebi.ac.uk/pdbsum/7aae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aae ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7aae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aae OCA], [https://pdbe.org/7aae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aae RCSB], [https://www.ebi.ac.uk/pdbsum/7aae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aae ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Angelini | [[Category: Angelini A]] | ||
[[Category: Cendron | [[Category: Cendron L]] | ||
[[Category: Liberi | [[Category: Liberi S]] | ||
[[Category: Maso | [[Category: Maso L]] | ||
[[Category: Trande | [[Category: Trande M]] | ||
Latest revision as of 16:24, 6 November 2024
Crystal structure of Human serum albumin in complex with myristic acid at 2.27 Angstrom ResolutionCrystal structure of Human serum albumin in complex with myristic acid at 2.27 Angstrom Resolution
Structural highlights
Publication Abstract from PubMedPerfluorooctanoic acid (PFOA) is a toxic compound that is absorbed and distributed throughout the body by noncovalent binding to serum proteins such as human serum albumin (hSA). Though the interaction between PFOA and hSA has been already assessed using various analytical techniques, a high resolution and detailed analysis of the binding mode is still lacking. We report here the crystal structure of hSA in complex with PFOA and a medium-chain saturated fatty acid (FA). A total of eight distinct binding sites, four occupied by PFOAs and four by FAs, have been identified. In solution binding studies confirmed the 4:1 PFOA-hSA stoichiometry and revealed the presence of one high and three low affinity binding sites. Competition experiments with known hSA-binding drugs allowed locating the high affinity binding site in sub-domain IIIA. The elucidation of the molecular basis of the interaction between PFOA and hSA might provide not only a better assessment of the absorption and elimination mechanisms of these compounds in vivo but also have implications for the development of novel molecular receptors for diagnostic and biotechnological applications. This article is protected by copyright. All rights reserved. Unveiling the binding mode of perfluorooctanoic acid to human serum albumin.,Maso L, Trande M, Liberi S, Moro G, Daems E, Linciano S, Sobott F, Covaceuszach S, Cassetta A, Fasolato S, Moretto LM, De Wael K, Cendron L, Angelini A Protein Sci. 2021 Feb 7. doi: 10.1002/pro.4036. PMID:33550662[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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